ID M9RIX0_9RHOB Unreviewed; 101 AA.
AC M9RIX0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Large ribosomal subunit protein uL24 {ECO:0000256|ARBA:ARBA00035206, ECO:0000256|HAMAP-Rule:MF_01326};
GN Name=rplX {ECO:0000256|HAMAP-Rule:MF_01326,
GN ECO:0000313|EMBL:AGI69775.1};
GN ORFNames=OAN307_c44070 {ECO:0000313|EMBL:AGI69775.1};
OS Octadecabacter antarcticus 307.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Octadecabacter.
OX NCBI_TaxID=391626 {ECO:0000313|EMBL:AGI69775.1, ECO:0000313|Proteomes:UP000005307};
RN [1] {ECO:0000313|EMBL:AGI69775.1, ECO:0000313|Proteomes:UP000005307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=307 {ECO:0000313|EMBL:AGI69775.1,
RC ECO:0000313|Proteomes:UP000005307};
RX PubMed=23671678;
RA Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA Brinkhoff T., Simon M., Daniel R.;
RT "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT Plasticity and a New Type of Xanthorhodopsin.";
RL PLoS ONE 8:E63422-E63422(2013).
CC -!- FUNCTION: One of the proteins that surrounds the polypeptide exit
CC tunnel on the outside of the subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01326}.
CC -!- FUNCTION: One of two assembly initiator proteins, it binds directly to
CC the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC subunit. {ECO:0000256|HAMAP-Rule:MF_01326}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01326}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL24 family.
CC {ECO:0000256|ARBA:ARBA00010618, ECO:0000256|HAMAP-Rule:MF_01326,
CC ECO:0000256|RuleBase:RU003477}.
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DR EMBL; CP003740; AGI69775.1; -; Genomic_DNA.
DR RefSeq; WP_015501689.1; NC_020911.1.
DR AlphaFoldDB; M9RIX0; -.
DR STRING; 391626.OAN307_c44070; -.
DR KEGG; oat:OAN307_c44070; -.
DR eggNOG; COG0198; Bacteria.
DR HOGENOM; CLU_093315_2_2_5; -.
DR OrthoDB; 9807419at2; -.
DR Proteomes; UP000005307; Chromosome.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd06089; KOW_RPL26; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR HAMAP; MF_01326_B; Ribosomal_L24_B; 1.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR014722; Rib_uL2_dom2.
DR InterPro; IPR003256; Ribosomal_uL24.
DR InterPro; IPR005825; Ribosomal_uL24_CS.
DR InterPro; IPR041988; Ribosomal_uL24_KOW.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR NCBIfam; TIGR01079; rplX_bact; 1.
DR PANTHER; PTHR12903:SF0; 39S RIBOSOMAL PROTEIN L24, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12903; MITOCHONDRIAL RIBOSOMAL PROTEIN L24; 1.
DR Pfam; PF00467; KOW; 1.
DR Pfam; PF17136; ribosomal_L24; 1.
DR SMART; SM00739; KOW; 1.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR PROSITE; PS01108; RIBOSOMAL_L24; 1.
PE 3: Inferred from homology;
KW Ribonucleoprotein {ECO:0000256|HAMAP-Rule:MF_01326,
KW ECO:0000256|RuleBase:RU003477};
KW Ribosomal protein {ECO:0000256|HAMAP-Rule:MF_01326,
KW ECO:0000256|RuleBase:RU003477};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01326};
KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01326}.
FT DOMAIN 4..31
FT /note="KOW"
FT /evidence="ECO:0000259|SMART:SM00739"
SQ SEQUENCE 101 AA; 10591 MW; 620069817C762D11 CRC64;
MAAKLRKGDN VIVLAGKDKG MTGEISSVDP KSGKAIVDGV NVAIRHVKQS QTTQGGRTPK
AMPIQLSNLA VVDANGKATR VGFKMDGDKK VRFAKTTGDV I
//